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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Although not a source of energy, cholesterol plays a significant role as a foundational structure for bile salts, steroid hormones, and vitamin D, as well as being a crucial component of plasma membranes. Approximately 15% of blood cholesterol is derived from our diet, with the remainder synthesized from acetyl CoA by the liver and intestines. Cholesterol is eliminated from the body through its conversion into bile salts, which are eventually discarded in the feces.
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There are numerous types of normal and abnormal respiration. Based on ventilatory movements, breathing patterns are classified as regular, deep, or shallow. Examples include Biot's breathing, Cheyne-Stokes respiration, Kussmaul's breathing, hyperventilation, and hypoventilation. Each pattern is clinically significant and aids in evaluating patients.
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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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High-throughput Nitrobenzoxadiazole-labeled Cholesterol Efflux Assay
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Specific Cholesterol Binding Drives Drastic Structural Alterations in Apolipoprotein A1.

Arjun Ray1,2, Asmita Ghosh1,2, Rahul Chakraborty1,2

  • 1CSIR-Institute of Genomics and Integrative Biology , South Campus, Mathura Road , New Delhi 110 025 , India.

The Journal of Physical Chemistry Letters
|September 27, 2018
PubMed
Summary
This summary is machine-generated.

Apolipoprotein A1 (ApoA1) monomers adopt a compact shape but form a circular structure when bound to cholesterol. This transformation is driven by specific N-terminal and C-terminal cholesterol binding sites.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Dynamics

Background:

  • High-density lipoprotein (HDL) and its main protein, apolipoprotein A1 (ApoA1), are crucial in lipid metabolism.
  • The structural dynamics of monomeric ApoA1, particularly its conformational flexibility, are not well understood.
  • Understanding ApoA1 structure is key to elucidating HDL assembly and function.

Purpose of the Study:

  • To investigate the structural properties and conformational changes of monomeric ApoA1.
  • To determine the role of cholesterol in modulating ApoA1 structure.
  • To identify the specific binding sites involved in cholesterol-induced structural alterations.

Main Methods:

  • Utilized extensive molecular simulations (over 50 μs) to model ApoA1 behavior.
  • Introduced physiological concentrations of cholesterol to simulated ApoA1 systems.
  • Performed complementary experimental validation to confirm simulation findings.

Main Results:

  • Monomeric ApoA1 adopts a compact conformation in simulations.
  • Cholesterol binding induces a spontaneous transition of ApoA1 to a circular conformation.
  • Specific cholesterol binding sites at the N-terminal and C-terminal regions were identified as key drivers of this structural change.
  • Mutating the N-terminal binding site prevented the formation of the open, belt-shaped topology.

Conclusions:

  • Cholesterol binding specifically induces significant structural changes in monomeric ApoA1.
  • ApoA1 undergoes a stepwise opening mechanism, facilitated by distinct N-terminal and C-terminal binding sites.
  • These findings provide novel insights into the structural plasticity of ApoA1 and its interaction with cholesterol, impacting HDL structure and function.